Energetic contributions to the initiation of transcription in E. coli.

The thermodynamics of RNA polymerase (RNAP) binding to a 108 base pair (bp) synthetic promoter with consensus sequences at the -35 and -10 bp binding regions upstream from the transcription start point were determined using isothermal titration calorimetry (ITC). The binding constant at 25 degrees C is 2.37+/-0.

Thermodynamics of single strand DNA base stacking.

The thermodynamics of the stacking to unstacking transitions of 24 single-stranded DNA sequences (ssDNA), 10-12 bases in length, in sodium phosphate buffer were determined from 10 to 95 degrees C, using differential scanning calorimetry (DSC). An additional 22 ssDNA sequences did not exhibit an S<=>U transition in this temperature range. The transition properties of the ssDNA sequences with View Article and Find Full Text PDF

Effect of the distal C162S mutation on the energetics of drug binding to p38alpha MAP kinase.

The binding reactions of the inhibitor drugs, SB 203580, SKF 86002, and p38 INH.1 to the isoforms 1 and 2 splice variants of p38alpha MAP kinase and their C162S mutants, as determined from ITC measurements from 25 to 35 degrees C, are totally enthalpically driven with binding constants ranging from 10(7)M(-1) for SKF 86002 and SB 203580 to 10(9)M(-1) for p38 INH.1.

Solution structure of HI1506, a novel two-domain protein from Haemophilus influenzae.

HI1506 is a 128-residue hypothetical protein of unknown function from Haemophilus influenzae. It was originally annotated as a shorter 85-residue protein, but a more detailed sequence analysis conducted in our laboratory revealed that the full-length protein has an additional 43 residues on the C terminus, corresponding with a region initially ascribed to HI1507. As part of a larger effort to understand the functions of hypothetical proteins from Gram-negative bacteria, and H.